ASL7_SARSH
ID ASL7_SARSH Reviewed; 1432 AA.
AC A0A2U8U2K9;
DT 26-FEB-2020, integrated into UniProtKB/Swiss-Prot.
DT 12-SEP-2018, sequence version 1.
DT 03-AUG-2022, entry version 18.
DE RecName: Full=ABC transporter asL7 {ECO:0000303|PubMed:29773797};
DE AltName: Full=Xenovulene A biosynthesis cluster protein L7 {ECO:0000303|PubMed:29773797};
GN Name=asL7 {ECO:0000303|PubMed:29773797};
OS Sarocladium schorii (Acremonium strictum (strain IMI 501407)).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Sarocladiaceae; Sarocladium;
OC unclassified Sarocladium.
OX NCBI_TaxID=2203296;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], INDUCTION, AND FUNCTION.
RX PubMed=29773797; DOI=10.1038/s41467-018-04364-9;
RA Schor R., Schotte C., Wibberg D., Kalinowski J., Cox R.J.;
RT "Three previously unrecognised classes of biosynthetic enzymes revealed
RT during the production of xenovulene A.";
RL Nat. Commun. 9:1963-1963(2018).
RN [2]
RP BIOTECHNOLOGY.
RX PubMed=9262310;
RA Thomas P., Sundaram H., Krishek B.J., Chazot P., Xie X., Bevan P.,
RA Brocchini S.J., Latham C.J., Charlton P., Moore M., Lewis S.J.,
RA Thornton D.M., Stephenson F.A., Smart T.G.;
RT "Regulation of neuronal and recombinant GABA(A) receptor ion channels by
RT xenovulene A, a natural product isolated from Acremonium strictum.";
RL J. Pharmacol. Exp. Ther. 282:513-520(1997).
RN [3]
RP FUNCTION.
RX PubMed=17912413; DOI=10.1039/b708614h;
RA Bailey A.M., Cox R.J., Harley K., Lazarus C.M., Simpson T.J., Skellam E.;
RT "Characterisation of 3-methylorcinaldehyde synthase (MOS) in Acremonium
RT strictum: first observation of a reductive release mechanism during
RT polyketide biosynthesis.";
RL Chem. Commun. (Camb.) 39:4053-4055(2007).
RN [4]
RP FUNCTION.
RX PubMed=20552126; DOI=10.1039/c0cc01162b;
RA Fisch K.M., Skellam E., Ivison D., Cox R.J., Bailey A.M., Lazarus C.M.,
RA Simpson T.J.;
RT "Catalytic role of the C-terminal domains of a fungal non-reducing
RT polyketide synthase.";
RL Chem. Commun. (Camb.) 46:5331-5333(2010).
CC -!- FUNCTION: ABC transporter; part of the gene cluster that mediates the
CC biosynthesis of xenovulene A, an unusual meroterpenoid that has potent
CC inhibitory effects on the human gamma-aminobutyrate A (GABAA)
CC benzodiazepine receptor. {ECO:0000269|PubMed:29773797}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- INDUCTION: Expression is significantly up-regulated under xenovulene A
CC producing condition. {ECO:0000269|PubMed:29773797}.
CC -!- BIOTECHNOLOGY: Xenovulene A is a natural product exhibiting little
CC structural resemblance with classical benzodiazepines yet is able to
CC displace high-affinity ligand binding to the benzodiazepine site of the
CC gamma-aminobutyrate A (GABAA) receptor and could be potentially used as
CC an anti-depressant with reduced addictive properties.
CC {ECO:0000269|PubMed:9262310}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCG family.
CC PDR (TC 3.A.1.205) subfamily. {ECO:0000305}.
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DR EMBL; MG736817; AWM95783.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2U8U2K9; -.
DR SMR; A0A2U8U2K9; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0042626; F:ATPase-coupled transmembrane transporter activity; IEA:InterPro.
DR CDD; cd03233; ABCG_PDR_domain1; 1.
DR CDD; cd03232; ABCG_PDR_domain2; 1.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR013525; ABC_2_trans.
DR InterPro; IPR029481; ABC_trans_N.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR017871; ABC_transporter-like_CS.
DR InterPro; IPR034001; ABCG_PDR_1.
DR InterPro; IPR034003; ABCG_PDR_2.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR010929; PDR_CDR_ABC.
DR Pfam; PF01061; ABC2_membrane; 2.
DR Pfam; PF00005; ABC_tran; 2.
DR Pfam; PF14510; ABC_trans_N; 1.
DR Pfam; PF06422; PDR_CDR; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
PE 1: Evidence at protein level;
KW ATP-binding; Cell membrane; Glycoprotein; Membrane; Nucleotide-binding;
KW Repeat; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..1432
FT /note="ABC transporter asL7"
FT /id="PRO_0000449186"
FT TRANSMEM 450..470
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 484..504
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 530..550
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 559..579
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 597..617
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 702..722
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1135..1155
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1166..1186
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1215..1235
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1251..1271
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1279..1299
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1317..1337
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1402..1422
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 91..341
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 786..1029
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1076..1095
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 822..829
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT CARBOHYD 265
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1017
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1371
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 1432 AA; 161123 MW; A6F1B960F59EC6CC CRC64;
MFDTTKLQSS TQDGSTSSVT GEPIFGANDP NSELNPSSSH FNVRAWASNY AKVTLEGGSQ
FRRMGVCFQN LNAFGFITPA DYQKDVANIW LALPGMLIRN RKRVNILHQF DGIIRPGEMC
VVLGPPSSGC STFLKTLSGD RDGFFIGEDS YFNYEGISDK ELHTAHRGDA IYTAETDVHF
PKLTVSQTLE FAAQARCPRE IPQGIPRQQF CKQLKDVVMG MYGISHTADT KVGNDYIRGV
SGGERKRVTI AEATLSNAPL QCWDNCTRGL DSANAIGFCK TLRLQSEFFG QSCAVSMYQA
PQSAYDLFDK ATVLYQGHQI YFGPADEAKA YFERLGFECP SRQTTPDFLT SMTFPEERIT
RAGFNPPRTP EEFAAAWRSS PEYKALQTDI SEYKTKHPID GPNAGVYREL KKSYQARGQR
IKSPYTLTYM QQVQMCMRRA WNRLVSDPGP TIVVTMGNFV LALIMSSLFF NMQPDTDSFY
GREVVLFMAV MFNAFASVLE VMTLYAQRPI VEKQARYAFY HPSAEAYSSV LMDLPIKVLA
CVSFNLVFYF MTNLNRTPGN FFFYLLASFF IVLSMSGIFR FIKIPSAAFS RTVQQAMIPA
SILMVFLITF AGFMVPINYM LPWCRWINYL NPVAYGFESL MINEYAGREF RCSNYIPFDG
TPGDPNVACN VVGAVAGETF VSGDAHISEA YSYDAAHKWR NIGIVIAMTI FNYTMCFITS
EYVSAKKSKG EILVFRRGFV PKNTHVNKIT DDLEARSLPV TKIVESPEGS KEKVGGELQS
GSTSIFHWRN VCYDIKIKGK PRRILDNVDG WVKPGTMTAL MGVSGAGKTT LLDCLADRRT
GIGIITGEML VDGKIRDESF QRKTGYAQQQ DLHLETATVR ESLVFSALLR RPHHIPKAEK
LAYVEEVIDL LEMGPYADAV VGVLGEGLNV EQRKRLTIAV ELAAKPPLLL FVDEPTSGLD
SQTSWAVVNL LEKLSKAGQS ILCTLHQPSA MLFQRFDRLL LLADGGKTVY FGDIGENSST
LVEYFERKAK HPCPPNANPA EWMLEAIGAA PGTTSEVDWQ HVWRTSPEFD RVQEELSRLR
EHGSQSNSHD SEKSETKAVT YHGEFAVPLW TQFVVVIERV FQQSWRTPAY IYSRFALCGV
VSLFIGLVFL NSPLSVRGLQ NQMFAVFQLF AIVGQLVSQQ MPQFIIQRSL YEVRERPAKT
YSWKVFMVSQ ILSDIPYYAL ASVMMWALWY FPIGLYKNAE VAGQETERGA LMWLLFLAWL
MWVSTFGHFC ISFSETAEAG ANAANFMYVL VNFFCGALIT PNQMPRFWIF LYRASPLSYL
VSSMLSAGIA NVEVTCAANE YTIIDPPMGQ TCYEYLRNEI NTIGGYLLDN NATENCKFCK
LKYSNVFLSE IEIEYGTRWR NFGIIWVYVI FNISAAITLY WVARMPKGHR KV
